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ATP5MC1 | ATP synthase lipid-binding protein, mitochondrial; Belongs to the ATPase C chain family. (135 aa) | ||||
F7ALL9_MACMU | Uncharacterized protein. (256 aa) | ||||
ENSMMUP00000049207 | Uncharacterized protein. (95 aa) | ||||
ATP5ME | Uncharacterized protein. (221 aa) | ||||
ENSMMUP00000065714 | Uncharacterized protein. (192 aa) | ||||
ATP5PB | Uncharacterized protein. (290 aa) | ||||
ATP5MG | ATP synthase subunit; Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proto [...] (114 aa) | ||||
LOC699117 | Uncharacterized protein. (137 aa) | ||||
LOC707476 | ATP-synt_C domain-containing protein; Belongs to the ATPase C chain family. (135 aa) | ||||
ATP5PF | ATP synthase-coupling factor 6, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain; Belongs to the eukaryotic ATPase subunit F6 family. (116 aa) | ||||
ATP5MG-2 | Uncharacterized protein. (77 aa) | ||||
ATP5PD | ATP synthase subunit d, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the cent [...] (161 aa) |